Source:http://linkedlifedata.com/resource/pubmed/id/17586505
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-3
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pubmed:dateCreated |
2007-9-10
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pubmed:abstractText |
Crustacean hyperglycemic hormone (CHH) regulates carbohydrate metabolism, molting, and ion and water transport. cDNAs encoding four CHH isoforms (designated EG-CHH-A, -B, -C, and -D) were cloned from eyestalk ganglia (EG) from land crab, Gecarcinus lateralis. The isoforms differed in the 3' region of the open reading frame and/or the length of the 3' untranslated region. All encoded essentially identical preprohormones containing a 28-amino acid (aa) signal peptide, a 42-aa precursor related peptide and a 72-aa mature CHH. All deduced aa sequences had the six cysteines, two arginines, one aspartate, one phenylalanine, and one arginine originally identified as characteristic of this neuropeptide family. There was a single aa difference between the EG-CHH-D mature hormone and the other three isoforms. The EG-CHH isoforms were expressed in EG, hindgut, and thoracic ganglion. A fifth CHH isoform, designated pericardial organ (PO)-CHH, was similar to the PO-CHH isoform described in green crab, Carcinus maenas. It was expressed in hindgut and testis, but not in eyestalk ganglia; its expression in PO was not determined. The deduced aa sequence of the PO-CHH was identical to that of the EG-CHH isoforms through aa #40 of the mature peptide. The divergent aa sequence between positions #41 and #73 was encoded by an insertion of a 111-bp sequence absent in EG-CHH cDNAs. The data suggest that EG-CHH and PO-CHH isoforms are generated by alternative splicing of at least two CHH genes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arthropod Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Invertebrate Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/hyperglycemic hormone, crustacean
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pubmed:status |
MEDLINE
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pubmed:issn |
0016-6480
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
154
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
174-83
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:17586505-Amino Acid Sequence,
pubmed-meshheading:17586505-Animals,
pubmed-meshheading:17586505-Arthropod Proteins,
pubmed-meshheading:17586505-Base Sequence,
pubmed-meshheading:17586505-Brachyura,
pubmed-meshheading:17586505-Cloning, Molecular,
pubmed-meshheading:17586505-Invertebrate Hormones,
pubmed-meshheading:17586505-Molecular Sequence Data,
pubmed-meshheading:17586505-Nerve Tissue Proteins,
pubmed-meshheading:17586505-Protein Isoforms,
pubmed-meshheading:17586505-Sequence Homology, Amino Acid,
pubmed-meshheading:17586505-Tissue Distribution
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pubmed:articleTitle |
Crustacean hyperglycemic hormone from the tropical land crab, Gecarcinus lateralis: cloning, isoforms, and tissue expression.
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pubmed:affiliation |
Department of Biology, Colorado State University, Fort Collins, CO 80523, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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